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Assessment of glycanolytic enzymes producing potentialities of three strains of Penicillium sp
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Abstract
Microfungi are part of the microbiome that play a significant role in the decomposition of natural substances by producing various enzymes that have industrial relevance. The primary objective of the study is to determine the glycanolytic enzyme-producing potentialities of three microfungi strains, viz.PDF4, XDF1(i), and XDF7(iii), and to optimize the enzyme production and activity at different pH and temperatures. The strains were characterized by molecular methods. The enzyme production efficacy was tested both qualitatively and quantitatively using glycan molecules, such as carboxymethylcellulose (CMC), birchwood xylan, and pectin. The enzyme activities were evaluated under varying pH and temperature conditions to determine the optimal parameters for maximal enzyme activity. Additionally, the ability of the strains to degrade lignocellulosic substrates, such as sugarcane bagasse and musambi peel, and to synthesize those enzymes was also investigated. The studies revealed that among the strains belonging to
Penicillium citrinum
strain PDF4 (ITS: OR555780; NL: OR555752),
P. citrinum
strain XDF1(i) (ITS: OR555782; NL: OR555750), and
P. oxalicum
strain XDF7 (iii) (ITS: OR555781; NL: OR555751), strain XDF7(iii) was the highest pectinase producer (0.303547 µM/mL/min at pH 3.0), followed by PDF4 with 0.245313 µM/mL/min, and XDF1(i) with 0.205393 µM/mL/min, at pH 4.0 in YP-pectin medium. While XDF7(iii) showed the highest xylanase activity, reaching 0.768501µM/mL/min at pH 5.0, followed by 0.563401 µM/mL/min at pH 6.0. XDF1(i) exhibited the second-highest xylanase activity (0.553409µM/mL/min) at pH 5.0. In contrast, PDF4 recorded 0.343314 µM/mL/min xylanase activity at pH 5.0 in YP-xylan substrates, respectively, while strain XDF7(iii) demonstrated poor production of CMCase (0.01302 µM/mL/min) at pH 3.0, followed by XDF1(i) (0.0121µM/mL/min at pH 3.0) and PDF4 (0.00696 µM/mL/min) at pH 4.0 in YP-CMC medium at 7 days of fermentation at 37°C. The studies further revealed that the strain XDF7(iii) effectively utilized both musambi peel and sugarcane bagasse, and recorded the highest xylanase activity (1.0912764 µM/mL/min) on the 3rd day of incubation on lemon (Musambi) peel and the second-highest activity (0.9921957µM/mL/min) on the 7th day on sugarcane bagasse. While PDF4 produced the highest xylanase activity (0.7687782 µM/mL/min) on the 7th day, XDF1(i) exhibited only moderate xylanase activity on the 3rd day (0.5166818µM/mL/min). In contrast, CMCase activity remained minimal throughout the incubation period with Musambi peel. Thus, the study concludes that these new environmental strains of
Penicillium
sp. can produce a high amount of industrial enzymes, such as xylanase and pectinase, under standard fermentation conditions. This suggests that they could be utilized as low-cost enzymes from lignocellulose biomasses and also for lignocellulose biomass bioconversion to develop numerous value-added products.
Springer Science and Business Media LLC
Title: Assessment of glycanolytic enzymes producing potentialities of three strains of Penicillium sp
Description:
Abstract
Microfungi are part of the microbiome that play a significant role in the decomposition of natural substances by producing various enzymes that have industrial relevance.
The primary objective of the study is to determine the glycanolytic enzyme-producing potentialities of three microfungi strains, viz.
PDF4, XDF1(i), and XDF7(iii), and to optimize the enzyme production and activity at different pH and temperatures.
The strains were characterized by molecular methods.
The enzyme production efficacy was tested both qualitatively and quantitatively using glycan molecules, such as carboxymethylcellulose (CMC), birchwood xylan, and pectin.
The enzyme activities were evaluated under varying pH and temperature conditions to determine the optimal parameters for maximal enzyme activity.
Additionally, the ability of the strains to degrade lignocellulosic substrates, such as sugarcane bagasse and musambi peel, and to synthesize those enzymes was also investigated.
The studies revealed that among the strains belonging to
Penicillium citrinum
strain PDF4 (ITS: OR555780; NL: OR555752),
P.
citrinum
strain XDF1(i) (ITS: OR555782; NL: OR555750), and
P.
oxalicum
strain XDF7 (iii) (ITS: OR555781; NL: OR555751), strain XDF7(iii) was the highest pectinase producer (0.
303547 µM/mL/min at pH 3.
0), followed by PDF4 with 0.
245313 µM/mL/min, and XDF1(i) with 0.
205393 µM/mL/min, at pH 4.
0 in YP-pectin medium.
While XDF7(iii) showed the highest xylanase activity, reaching 0.
768501µM/mL/min at pH 5.
0, followed by 0.
563401 µM/mL/min at pH 6.
XDF1(i) exhibited the second-highest xylanase activity (0.
553409µM/mL/min) at pH 5.
In contrast, PDF4 recorded 0.
343314 µM/mL/min xylanase activity at pH 5.
0 in YP-xylan substrates, respectively, while strain XDF7(iii) demonstrated poor production of CMCase (0.
01302 µM/mL/min) at pH 3.
0, followed by XDF1(i) (0.
0121µM/mL/min at pH 3.
0) and PDF4 (0.
00696 µM/mL/min) at pH 4.
0 in YP-CMC medium at 7 days of fermentation at 37°C.
The studies further revealed that the strain XDF7(iii) effectively utilized both musambi peel and sugarcane bagasse, and recorded the highest xylanase activity (1.
0912764 µM/mL/min) on the 3rd day of incubation on lemon (Musambi) peel and the second-highest activity (0.
9921957µM/mL/min) on the 7th day on sugarcane bagasse.
While PDF4 produced the highest xylanase activity (0.
7687782 µM/mL/min) on the 7th day, XDF1(i) exhibited only moderate xylanase activity on the 3rd day (0.
5166818µM/mL/min).
In contrast, CMCase activity remained minimal throughout the incubation period with Musambi peel.
Thus, the study concludes that these new environmental strains of
Penicillium
sp.
can produce a high amount of industrial enzymes, such as xylanase and pectinase, under standard fermentation conditions.
This suggests that they could be utilized as low-cost enzymes from lignocellulose biomasses and also for lignocellulose biomass bioconversion to develop numerous value-added products.
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